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Neisseria gonorrhoeae Search Results

Record: 1 of 1  
MiniMap tRNA-His-1 tRNA-Arg-5 tRNA-Pro-3 IGR1642 IGR1640 IGR1645 IGR1643 IGR1641 IGR1644 IGR1646 folD, - NG1999 asd, - NG1997 NG2000 NG1996 NG1998 exoA, - NG1994 ngoI,dcm, - NG1991 dcrA, - NG1992 cysS, - NG1993 bvg,birA, - NG2001 folD, - NG1999 asd, - NG1997 NG2000 NG1996 NG1998 exoA, - NG1994 ngoI,dcm, - NG1991 dcrA, - NG1992 cysS, - NG1993 bvg,birA, - NG2001 folD, - NG1999 asd, - NG1997 NG2000 NG1998 exoA, - NG1994 dcrA, - NG1992 cysS, - NG1993 bvg,birA, - NG2001 NG1995 NG1996 ngoI,dcm, - NG1991 NG1995
* Calculated from Protein Sequence

Gene ID: NG1997

DNA Molecule Name:
1  

Genbank ID:


Gene Name:
asd  

Definition:
aspartate-semialdehyde dehydrogenase

Gene Start:
1970437

Gene Stop:
1969325

Gene Length:
1113

Molecular Weight*:
39825

pI*:
5.40

Net Charge*:
-4.45

EC:
1.2.1.11  

Functional Class:
Amino acid biosynthesis; Aspartate family  
Fatty acid and phospholipid metabolism  

Pathway: pathway table
Glycine, serine and threonine metabolism
Lysine biosynthesis

Secondary Evidence:
Hoang,T.T., Williams,S., Schweizer,H.P. and Lam,J.S.
Molecular genetic analysis of the region containing the essential
Pseudomonas aeruginosa asd gene encoding
aspartate-beta-semialdehyde dehydrogenase
Microbiology 143 (Pt 3), 899-907 (1997)
Medline: 97237719

Haziza,C., Stragier,P. and Patte,J.C.
Nucleotide sequence of the asd gene of Escherichia coli: absence of a typical attenuation signal.
EMBO J. 1 (3), 379-384 (1982)
Medline: 84182485

Arps,P.J. and Winkler,M.E.
Structural analysis of the Escherichia coli K-12 hisT operon by using a kanamycin resistance cassette
J. Bacteriol. 169 (3), 1061-1070 (1987)
MEDLINE: 87137258

Karsten,W.E. and Viola,R.E.
Identification of an essential cysteine in the reaction catalyzed by aspartate-beta-semialdehyde dehydrogenase
from Escherichia coli
Biochim. Biophys. Acta 1121 (1-2), 234-238 (1992)
MEDLINE: 92287957

Hadfield,A., Kryger,G., Ouyang,J., Petsko,G.A., Ringe,D. and Viola,R.
Structure of aspartate-beta-semialdehyde
dehydrogenase from Escherichia coli, a key enzyme in the aspartate family of amino acid biosynthesis
J. Mol. Biol. 289 (4), 991-1002 (1999)
MEDLINE: 99299393


Comment:
Oklahoma ID: NGO.1997c

Blast Summary:  PSI-Blast Search
NG1997 is 100% identical to a previously sequenced N.gonorrhoeae protein in GenBank, 11323196, a predicted aspartate-semialdehyde b-dehydrogenase.

Several hits in gapped BLAST to Asd sequences. Residues 2-368 are 68% similar to the enzyme in P.aeruginosa (gb|AAG06505).

Residues 1-371 are virtually identical to NMA0351 in N.meningitidis (AL162752).



COGS Summary:  COGS Search
BeTs to 11 clades of COG0136
COG name: Aspartate-semialdehyde dehydrogenase
Functional Class:  E
The phylogenetic pattern of COG0136 is amtkyqvcEbrHuj----inx
Number of proteins in this genome belonging to this COG is 1

Blocks Summary:  Blocks Search
***** IPB000319 (Aspartate-semialdehyde dehydrogenase) with a combined E-value of 3.1e-51.
    IPB000319A    3-14
    IPB000319B    34-43
    IPB000319C    64-80
    IPB000319D    94-115
    IPB000319E    158-168
    IPB000319F    241-254
    IPB000319G    262-282
    IPB000319H    317-336
    IPB000319I    350-364
***** IPB000534 (Semialdehyde dehydrogenase) with a combined E-value of 1.1e-06.
    IPB000534A    130-147
    IPB000534B    265-277
    IPB000534A    67-84
    IPB000534B    350-362


ProDom Summary:  Protein Domain Search
Residues 160-363 are 33% similar to a (DEHYDROGENASE ASPARTATE-SEMIALDEHYDE ASA OXIDOREDUCTASE) protein domain (PD002095) which is seen in DHAS_CAMJE.

Residues 128-365 are 69% similar to a (ASPARTATE-SEMIALDEHYDE DEHYDROGENASE ASA OXIDOREDUCTASE) protein domain (PD011448) which is seen in DHAS_HAEIN.

Residues 3-127 are 67% similar to a (DEHYDROGENASE OXIDOREDUCTASE BIOSYNTHESIS NADP) protein domain (PD001262) which is seen in DHAS_ECOLI.



Paralogs:  Local Blast Search


NG1997 has no significant similarity (blastp p-value < 1e-3) to any other gene in this genome.


Pfam Summary:  Pfam Search
Residues 1 to 131 (E-value = 9.7e-37) place NG1997 in the Semialdhyde_dh family which is described as Semialdehyde dehydrogenase, NAD binding domain (PF01118)
Residues 144 to 354 (E-value = 1.1e-69) place NG1997 in the Semialdhyde_dhC family which is described as Semialdehyde dehydrogenase, dimerisation domain (PF02774)

Structural Feature(s):
Feature Type  Start  Stop
No predicted structural features.  
  

PDB Hit:
pdb|1MB4|1MB4-A CRYSTAL STRUCTURE OF ASPARTATE SEMIALDEHYDE 506.0 0e+00
pdb|1BRM|1BRM-A ASPARTATE BETA-SEMIALDEHYDE DEHYDROGENASE FROM 500.0 0e+00
pdb|1MB4|1MB4-A CRYSTAL STRUCTURE OF ASPARTATE SEMIALDEHYDE 672.0 0.000000
pdb|1BRM|1BRM-A AS

Gene Protein Sequence:
MKVGFVGWRGMVGSVLMQRMKEENDFAHIPEAFFFTSSNVGGAAPDFGQA
AKTLLDANDVAELAKMDIIVTCQGGDYTKSVFQALRDSGWNGYWIDAASS
LRMKDDAIIALDPVNRNVIDNGLKNGVKNYIGGNCTVSLMLMALGGLFQN
DLVEWATSMTYQAASGAGAKNMRELISGMGAIHAQVADELADPSSAILDI
DRKVSDFLRSEDYPKANFGVPLAGSLIPWIDVDLGNGQSKEEWKGGVETN
KILGRSGNPTVIDGLCVRIGAMRCHSQAITLKLKKDLPVSEIEAILAGAN
DWVKVVPNEKEAGIRELTPAKVTGTLSVPVGRIRKLGMGGEYISAFTVGD
QLLWGAAEPMRRVLRIVLGSL

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAGTAGGTTTCGTCGGCTGGCGCGGTATGGTCGGTTCGGTTTTGAT
GCAGCGTATGAAAGAAGAAAACGACTTCGCCCACATTCCCGAAGCGTTTT
TCTTTACCTCTTCCAACGTCGGCGGCGCGGCACCTGATTTCGGTCAGGCG
GCTAAAACATTATTGGACGCGAACGACGTTGCCGAGCTGGCGAAAATGGA
CATTATCGTCACCTGCCAAGGCGGCGATTACACCAAATCCGTCTTCCAAG
CCCTGCGCGACAGCGGCTGGAACGGCTACTGGATTGACGCGGCGTCCTCA
CTGCGCATGAAAGACGACGCGATTATCGCCCTCGACCCCGTCAACCGCAA
CGTCATCGACAACGGTCTCAAAAACGGCGTGAAAAACTACATCGGCGGCA
ACTGTACCGTCTCCCTGATGCTGATGGCTTTGGGCGGCCTGTTCCAAAAC
GATTTGGTCGAATGGGCGACCAGCATGACCTACCAAGCCGCTTCCGGCGC
GGGCGCGAAAAATATGCGCGAACTCATCAGCGGCATGGGCGCGATTCACG
CCCAAGTGGCGGACGAGCTTGCCGATCCTTCCAGCGCGATTCTCGATATC
GACCGCAAAGTGTCCGATTTCCTCCGCAGCGAAGACTATCCGAAAGCCAA
CTTCGGCGTACCGCTCGCCGGCAGCCTGATTCCGTGGATTGACGTGGATT
TGGGCAACGGCCAGTCCAAAGAAGAATGGAAGGGCGGCGTGGAAACCAAC
AAAATCCTCGGACGCAGCGGCAATCCGACCGTCATCGACGGCCTGTGCGT
CCGCATCGGCGCGATGCGCTGCCACAGCCAAGCCATCACTCTGAAGTTGA
AAAAAGACCTGCCTGTTTCCGAAATCGAAGCGATTTTGGCAGGCGCGAAC
GACTGGGTGAAAGTCGTCCCCAACGAAAAAGAAGCCGGCATCCGCGAGCT
GACGCCCGCCAAAGTTACCGGCACGCTGTCCGTCCCTGTCGGACGCATCC
GCAAACTGGGCATGGGCGGCGAATACATCAGCGCGTTCACCGTCGGCGAC
CAACTTTTGTGGGGTGCAGCCGAACCGATGCGCCGCGTGTTGCGTATCGT
GTTGGGCAGCCTG


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